| Primary Identifier | IPR030616 | Type | Family |
| Short Name | Aur |
| description | Aurora kinase was discovered by Glover and colleagues in a screen for genes required to maintain the centrosome cycle in Drosophila []. Its yeast homologue Ipl1 (also known as spindle assembly checkpoint kinase) was found to regulate chromosome segregation []. Subsequently, three mammal Aurora kinases, Aurora A, B and C, have been identified. They are highly conserved serine/threonine kinases that regulate chromosomal alignment and segregation during mitosis and meiosis []. They all contain a protein kinase domain and a destruction box (D-box) recognised by the multi-subunit E3-ubiquitin ligase anaphase promoting complex/cyclosome (APC/C), which mediates their proteasomal degradation. However, their N-terminal domains share little sequence identity and confer unique protein-protein interaction abilities among the Aurora kinases []. Functionally, Aurora A associates with centrosome, while Aurora B and Aurora C are parts of the chromosome passenger complex (CPC) [, ]. Aurora C plays a role in the meiotic cell cycle, but does not seem to be essential for cell divisions in somatic cells []. This entry also includes a number of uncharacterised proteins, predominantly from bacteria. |
